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Updated: Feb 27, 2026

Production, Crystallization, and Structure Determination of the IKK-binding Domain of NEMO
Published on: December 28, 2019
Crystal structure of the tricellulin C-terminal coiled-coil domain reveals a unique mode of dimerization
Anja Schuetz1, Veselina Radusheva1, Susanne M Krug2
1Helmholtz Protein Sample Production Facility, Max Delbrück Center for Molecular Medicine, Berlin, Germany.
Abstract:
Tricellulin is a tight junction protein localized to tricellular contacts in many epithelial tissues, where it is required for full barrier control. Here, we present crystal structures of the tricellulin C-terminal coiled-coil domain, revealing a potential dimeric arrangement. By combining structural, biochemical, functional, and mutation analyses, we gain insight into the mode of tricellulin oligomerization and suggest a model where dimerization of its cytoplasmic C-terminus may play an auxiliary role in stabilizing homophilic and potentially also heterophilic cis-interactions within tight junctions.
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